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Conserved domains on  [gi|1994458830|ref|WP_205256191|]
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SRPBCC family protein [Nakamurella flavida]

Protein Classification

SRPBCC family protein( domain architecture ID 51693)

SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may have a deep hydrophobic ligand-binding pocket

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 21-147 2.67e-35

START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


The actual alignment was detected with superfamily member cd07819:

Pssm-ID: 472699  Cd Length: 140  Bit Score: 119.65  E-value: 2.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994458830  21 AIADFRSYPEWAGAVKTVEVTDPGQGGRAAQVRFSMDAGPIKDTYELAYQWaADDRSVSWTLVKGQLQKAQRGSYVLRPV 100
Cdd:cd07819    20 VLADVEAYPEWSPKVKSVEVLLRDNDGRPEMVRIGVGAYGIKDTYALEYTW-DGAGSVSWTLVEGEGNRSQEGSYTLTPK 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1994458830 101 ApvDGaphTEVVYTLAVDLSIPLIGVFRRKAEKVVMDTALKELRKRV 147
Cdd:cd07819    99 G--DG---TRVTFDLTVELTVPLPGFLKRKAEPLVLDEALKGLKKRV 140
 
Name Accession Description Interval E-value
SRPBCC_2 cd07819
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 21-147 2.67e-35

Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


Pssm-ID: 176861  Cd Length: 140  Bit Score: 119.65  E-value: 2.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994458830  21 AIADFRSYPEWAGAVKTVEVTDPGQGGRAAQVRFSMDAGPIKDTYELAYQWaADDRSVSWTLVKGQLQKAQRGSYVLRPV 100
Cdd:cd07819    20 VLADVEAYPEWSPKVKSVEVLLRDNDGRPEMVRIGVGAYGIKDTYALEYTW-DGAGSVSWTLVEGEGNRSQEGSYTLTPK 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1994458830 101 ApvDGaphTEVVYTLAVDLSIPLIGVFRRKAEKVVMDTALKELRKRV 147
Cdd:cd07819    99 G--DG---TRVTFDLTVELTVPLPGFLKRKAEPLVLDEALKGLKKRV 140
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 25-146 6.56e-11

Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442114  Cd Length: 137  Bit Score: 56.41  E-value: 6.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994458830  25 FRSYPEWAGAVKTVEVTDpgQGGRAAQVRFSMDAGPIKDTYELAYQWAADdRSVSWTLVKGQLqKAQRGSYVLRPVApvD 104
Cdd:COG2867    24 VERYPEFLPWCKAARVLE--RDGDEVVAELTVSFKGLRESFTTRNTLDPP-ERIDFELVDGPF-KHLEGRWRFEPLG--E 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1994458830 105 GAphTEVVYTLAVDLSIPLIGVFRRKAEKVVMDTALKELRKR 146
Cdd:COG2867    98 GG--TKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFKKR 137
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 25-148 1.75e-05

Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. It also includes other proteins of the START superfamily.


Pssm-ID: 431388  Cd Length: 139  Bit Score: 42.09  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994458830  25 FRSYPEWAGAVKTVEVTDPGQ--GGRAAQVRFSMDAGPIKDTYelaYQWAADDRSVSWTLVKGQLQKAQRGSYVLRPVap 102
Cdd:pfam10604  19 FENWPRWHPGVLRVELEGGGGplRGVVGTLRVGGRRGTVREEL---VEYDPAPRLLAYRIVEPLGVANYVGTWTVTPA-- 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1994458830 103 vdgAPHTEVVYTLAVDLSIPLIGVFRRKAEKVV---MDTALKELRKRVE 148
Cdd:pfam10604  94 ---GGGTRVTWTGEFDGPPLGGPFRDPAAARAVkgdYRAGLDRLKAVLE 139
 
Name Accession Description Interval E-value
SRPBCC_2 cd07819
Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized ...
 21-147 2.67e-35

Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins; Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


Pssm-ID: 176861  Cd Length: 140  Bit Score: 119.65  E-value: 2.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994458830  21 AIADFRSYPEWAGAVKTVEVTDPGQGGRAAQVRFSMDAGPIKDTYELAYQWaADDRSVSWTLVKGQLQKAQRGSYVLRPV 100
Cdd:cd07819    20 VLADVEAYPEWSPKVKSVEVLLRDNDGRPEMVRIGVGAYGIKDTYALEYTW-DGAGSVSWTLVEGEGNRSQEGSYTLTPK 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1994458830 101 ApvDGaphTEVVYTLAVDLSIPLIGVFRRKAEKVVMDTALKELRKRV 147
Cdd:cd07819    99 G--DG---TRVTFDLTVELTVPLPGFLKRKAEPLVLDEALKGLKKRV 140
PasT COG2867
Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ...
 25-146 6.56e-11

Ribosome association toxin PasT (RatA) of the RatAB toxin-antitoxin module [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442114  Cd Length: 137  Bit Score: 56.41  E-value: 6.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994458830  25 FRSYPEWAGAVKTVEVTDpgQGGRAAQVRFSMDAGPIKDTYELAYQWAADdRSVSWTLVKGQLqKAQRGSYVLRPVApvD 104
Cdd:COG2867    24 VERYPEFLPWCKAARVLE--RDGDEVVAELTVSFKGLRESFTTRNTLDPP-ERIDFELVDGPF-KHLEGRWRFEPLG--E 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1994458830 105 GAphTEVVYTLAVDLSIPLIGVFRRKAEKVVMDTALKELRKR 146
Cdd:COG2867    98 GG--TKVTFDLDFEFKSPLLGALLGPVFNEAARRMVDAFKKR 137
Polyketide_cyc2 pfam10604
Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases ...
 25-148 1.75e-05

Polyketide cyclase / dehydrase and lipid transport; This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. It also includes other proteins of the START superfamily.


Pssm-ID: 431388  Cd Length: 139  Bit Score: 42.09  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994458830  25 FRSYPEWAGAVKTVEVTDPGQ--GGRAAQVRFSMDAGPIKDTYelaYQWAADDRSVSWTLVKGQLQKAQRGSYVLRPVap 102
Cdd:pfam10604  19 FENWPRWHPGVLRVELEGGGGplRGVVGTLRVGGRRGTVREEL---VEYDPAPRLLAYRIVEPLGVANYVGTWTVTPA-- 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1994458830 103 vdgAPHTEVVYTLAVDLSIPLIGVFRRKAEKVV---MDTALKELRKRVE 148
Cdd:pfam10604  94 ---GGGTRVTWTGEFDGPPLGGPFRDPAAARAVkgdYRAGLDRLKAVLE 139
PYR_PYL_RCAR_like cd07821
Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid ...
 25-148 1.29e-03

Pyrabactin resistance 1 (PYR1), PYR1-like (PYL), regulatory component of abscisic acid receptors (RCARs), and related proteins; The PYR/PYL/RCAR-like family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. PYR/PYL/RCAR plant proteins are receptors involved in signal transduction. They bind abscisic acid (ABA) and mediate its signaling. ABA is a vital plant hormone, which regulates plant growth, development, and response to environmental stresses. Upon binding ABA, these plant proteins interact with a type 2C protein phosphatase (PP2C), such as ABI1 and ABI2, and inhibit their activity. When ABA is bound, a loop (designated the gate/CL2 loop) closes over the ligand binding pocket, resulting in the weakening of the inactive PYL dimer and facilitating type 2C protein phosphatase binding. In the ABA:PYL1:ABI1 complex, the gate blocks substrate access to the phosphatase active site. A conserved Trp from PP2C inserts into PYL to lock the receptor in a closed formation. This group also contains Methylobacterium extorquens AM1 MxaD. The mxaD gene is located within the mxaFJGIR(S)ACKLDEHB cluster which encodes proteins involved in methanol oxidation. MxaD may participate in the periplasmic electron transport chain for oxidation of methanol. Mutants lacking MxaD exhibit a reduced growth on methanol, and a lower rate of respiration with methanol.


Pssm-ID: 176863 [Multi-domain]  Cd Length: 140  Bit Score: 36.92  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994458830  25 FRSYPEWAGAVKTVEVTDPGQG-GRAAQVRFSmDAGPIKdtyELAYQWAADDRSVSWTLVKGQL-QKAQRGSYVLRPVap 102
Cdd:cd07821    23 FGGLHKWHPAVASCELEGGGPGvGAVRTVTLK-DGGTVR---ERLLALDDAERRYSYRIVEGPLpVKNYVATIRVTPE-- 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1994458830 103 vdGAPHTEVVYTLAVDLSIPLIGVFRRKAEKVVMDTALKELRKRVE 148
Cdd:cd07821    97 --GDGGTRVTWTAEFDPPEGLTDELARAFLTGVYRAGLAALKAALE 140
SRPBCC cd07812
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 25-147 3.76e-03

START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


Pssm-ID: 176854  Cd Length: 141  Bit Score: 35.76  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994458830  25 FRSYPEWAGAVKTVEVTDPGQGGRAAQVRFSMDAGPIKD-TYELayQWAADDRSVSWTLVKGQLQKAQRGSYVLRPvapv 103
Cdd:cd07812    21 PERWPEWSPGLERVEVLGGGEGGVGARFVGGRKGGRRLTlTSEV--TEVDPPRPGRFRVTGGGGGVDGTGEWRLEP---- 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1994458830 104 DGAPHTEVVYTLAVDLSIPLIGVFRRKAEKVV---MDTALKELRKRV 147
Cdd:cd07812    95 EGDGGTRVTYTVEYDPPGPLLKVFALLLAGALkreLAALLRALKARL 141
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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